Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria

Journal of Molecular Biology

Volumn 426, Issue 24, 2014, Pages 4087-4098

  Koch, Johanna R ^a   Schmid, Franz X ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

disulfide relay; mitochondrial disulfide formation; mitochondrial import; mitochondrial intermembrane space; oxidative protein folding

Indexed keywords

CARRIER PROTEIN; CATION TRANSPORT PROTEIN; CHAPERONE; COX17 PROTEIN, S CEREVISIAE; DISULFIDE; MIA40 PROTEIN, S CEREVISIAE; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; SACCHAROMYCES CEREVISIAE PROTEIN; THIOL DERIVATIVE;

BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; ISOMERISM; KINETICS; METABOLISM; MISSENSE MUTATION; OXIDATION REDUCTION REACTION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

BIOCATALYSIS; CATION TRANSPORT PROTEINS; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ISOMERISM; KINETICS; MITOCHONDRIAL MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MUTATION, MISSENSE; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY; SULFHYDRYL COMPOUNDS;

EID: 84914145323     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.10.022     Document Type: Article

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